full length review

monomers

single subunits or blocks

polymer

larger molecule made up of many monomers; joined by covalent bonds

dehydration synthesis

the process of joining two molecules by removing water, forming covalent bonds. (water is outside after rxn)

hydrolysis reaction

the process of breaking down a polymer into monomers by adding water, which cleaves the covalent bonds. (water is now in the molecules)

carbohydrates examples

sugar, starch, glucose, glycogen, cellulose

carbohydrates monomer

monosaccaride eleme

elements contained in carbohydrates

carbon, hydrogen, and oxygen

function of carbohydrates

store energy and building material

starch

a polysaccharide found in plants; used for building material

glycogen

polysaccharide found in animals; used for building material

examples of polysaccharides acting as building blocks

1. cellulose for plant cell walls

2. chitin is by arthropods to build exoskeletons

monomer of nucleic acid

nucleotides

function of nucleic acid

store hereditary information

what elements does nucleic acids contain

carbon, hydrogen, oxygen, phosphorus, and nitrogen

nucleotide

sugar + phosphate + nitrogen

nucleoside

sugar + nitrogen base

monomer for protein

amino acids

what elements are in proteins

carbon, hydrogen, oxygen, nitrogen, sulfur

what is the side chain also called

the R chain

different groups of amino acids

are classified based on their side chains, which can be polar, nonpolar, acidic, or basic, influencing their properties and functions.

levels of protein structure

1. primary

2. secondary

3. tertiary

4. quaternary

primary structure

the unique sequence of amino acids in a polypeptide chain, determining the protein's identity and function.

secondary structure

the local folded structures that form within a protein due to hydrogen bonding between amino acids, primarily including alpha helices and beta sheets.

tertiary structure

structure refers to the overall three-dimensional shape of a protein, formed by interactions between the R groups of the amino acids, including hydrogen bonds, ionic bonds, and hydrophobic interactions.

quaternary structure

the structure formed by the assembly of multiple polypeptide chains, resulting in a functional protein complex.

lipids are ____ to water

hydrophobic

why are lipids hydrophobic

consist mostly of hydrocarbon, forming nonpolar covalent bonds

what elements do lipids contain

hydrogen, carbon, and oxygen

examples of lipids

fats, phospholipids, and steroids

example of proteins

Include enzymes, antibodies, and collagen.

examples of nucleic acid

DNA and RNA

purpose of fats

to store energy

saturated fatty acids

1. have no double bonds

2. solid at room temperature

3. ex. most animal fats

unsaturated fatty acids

1. have one or more double bonds

2. ex. plant fats and fish fats

3. liquid at room temperature

steroids

lipids characterized by a carbon skeleton consisting of four fused rings

phopholipids

two fatty acids and phosphate group are attached to glycerol

fatty acid tails are _____

hydrophobic (no water)

phosphate head is _____

hydrophilic (likes water)

phospholipid bilayer

a double layer of phospholipids that forms the basis of cell membranes, allowing selective permeability to substances.

metabolism

totality of an organism’s chemical reaction

catabolic pathways

breaking down complex molecules into simpler compounds; releases energy

anabolic pathways

building complex molecules from simpler ones; consume/require energy

free energy (G) measures

portion of a system’s energy that can perform work

exergonic reactions ____ free energy

release; product’s G < reactant’s G; - delta G == free energy RELEASED

delta G formula

delta G = gFinal - gInitial

endergonic reactions _____ free energy

absorb; product’s G > reactant’s G; + delta G == free energy REQUIRED

energy coupling

exogonic process to drive an endergonic one

ATP

hydrolysis breaks apart phosphate groups’ bonds; energy released (exergonic) and used for endergonic rxns in the cell

ADP

when ATP is hydrolyzed

activation energy

initial amount of energy the reactants need to absorb to become products

enzymes

proteins that act as biological catalysts; speeds up rxns w/o being used up

how do enzymes speed up metabolic rxns

by lowering the activation energy; do NOT affect delta G of the reaction

substrate

reactants

active site

region on enzyme where substrate binds to

induced fit

binding of substrate to active site

enzyme name

ends in -ase; usually refer to the substrate they bind to / type of reaction they catalyze; ex. lactase catalyzes the hydrolysis of lactose into glucose and galctose

what can denature an enzyme

pH and temp

enzymes’ structure

a sequence of amino acids; folds into specific shape; shape allows for binding to reactants

cofactors

non protein enzyme helps (ex. minerals)

coenzymes

organic cofactors (ex. vitamins)

competitive inhibitor

binds to active site; competes with substrate

noncompetitive inhibitor

binds to another part of the enzyme; enzyme changes shape; active site is nonfunctional

active / inactive conformations

enzymes that can be turned on or off

allosteric regulation

where a protein’s function at one site is affected by binding of a regulatory molecule at another site; can either activate or inhibit

cellular respiration

set of metabolic rxns and processes that take place in the cells to convert biochemical energy from carbs into ATP and then release waste products

respiration formula

C6H12O6 + 6O2 →6CO2 + ATP

aerobic ___ oxygen

requires

anaerobic _____ oxygen

does not require

stages of aerobic respiration

1. glycolysis

2. *intermediate step

3. krebs cycle (citric acid cycle)

4. oxidative phosphorylation

what are the reactant(s) of glycolysis

six-carbon glucose

products of glycolysis

two three-carbon pyruvate, net yield of 2 ATP and 2 NADH (products four but uses two)

setting for glycolysis

cytoplasm

part one of glycolysis: energy investment stage

uses ATP to phosphorylate (add phosphate group) compounds of glucose

part two of glycolysis: energy payoff stage

two three-carbon pyruvate oxidizes (loses electrons); generates 4 ATP and NAD+ is converted to NADH

product of one glucose molecule

2 net ATP; 2 NAD+ → NADH (electron carrier)

name for intermediate step

pyruvate oxidation

what happens during intermediate step (pyruvate oxidation)

pyruvate is transported into mitochondria to the matrix (fluid of mitochondria)

what does pyruvate convert to during intermediate step (pyruvate oxidation)

acetyl CoA

what used during intermediate step (pyruvate oxidation)

pyruvate

what is released and produced during intermediate step (pyruvate oxidation)

Co2 is released, 2 NADH are produced

what is the second stage (after intermediate) called for aerobic process

krebs cycle (citric acid cycle)

where does krebs cycle occur

mitochondria matrix

what is used for krebs cycle

acetyl CoA

what is the product of krebs cycle

(for two cycles) co2 waste, 2 atp, 6 NADH, 2 FADH2

what is the third stage called for aerobic process (after krebs cycle)

oxidative phosphorylation

where does oxidative phosphorylation occur

inner mitochondrial memebra

what are the two parts of oxidative phosphorylation called

electron transport chain and chemiosmosis

what does the electron transport chain use and what do those reactants produce

NADH and FADH2; releases electrons and H+ ions; the NAD+ and FAD+ can be reused and sent back to stage one

how does the products of the electron transport chain move

electrons are moved through the ETC and H+ is moved by proton pumps across inner mitochondrial membrane

what is a byproduct of ETC

h2o; does not make ATP directly

what is the second part of oxidative phosphorylation

chemiosmosis

what drives work for chemiosmosis

H+ gradient across membrane, moved by proton pumps

how many ATP is usually formed during chemiosmosis (second stage of oxidative phosphorylation)

30 - 34 ATP

what are the two common types of anaerobic respiration

1. alcohol fermentation

   1. lactic acid fermentation

what is pyruvate converted to during alcohol fermentation and its steps

ethanol;

1. 2 co2

   1. regenerates NAD+ so it can be reused by glycolysis

___ ATP net production of alcohol fermentation and examples

two; yeast cells

what is pyruvate reduced to by lactic acid fermentation

NADH, which regenerates NAD+

end product of lactic acid fermentation

lactate is end product; no release of co2

what are some examples of lactic acid fermentation

fungi; bacteria; to make cheese and yogurt

fermentation

keep glycolysis going by regenerating NAD+; occurs in cytosol; no oxygen needed; creates ethanol or 2 atp (from glycolysis)res